Journal article
The Arginine-Rich Domains Present in Human Immunodeficiency Virus Type 1 Tat and Rev Function as Direct Importin β-Dependent Nuclear Localization Signals
Abstract
Protein nuclear import is generally mediated by basic nuclear localization signals (NLSs) that serve as targets for the importin alpha (Imp alpha) NLS receptor. Imp alpha is in turn bound by importin beta (Imp beta), which targets the resultant protein complex to the nucleus. Here, we report that the arginine-rich NLS sequences present in the human immunodeficiency virus type 1 regulatory proteins Tat and Rev fail to interact with Imp alpha and …
Authors
Truant R; Cullen BR
Journal
Molecular and Cellular Biology, Vol. 19, No. 2, pp. 1210–1217
Publisher
Taylor & Francis
Publication Date
February 1, 1999
DOI
10.1128/mcb.19.2.1210
ISSN
0270-7306
Associated Experts
Fields of Research (FoR)
Medical Subject Headings (MeSH)
Amino Acid SequenceArginineBinding SitesGene Products, revGene Products, tatHIV-1HeLa CellsHumansIn Vitro TechniquesKaryopherinsNuclear Localization SignalsNuclear ProteinsProtein BindingRecombinant ProteinsSequence Homology, Amino Acidran GTP-Binding Proteinrev Gene Products, Human Immunodeficiency Virustat Gene Products, Human Immunodeficiency Virus